메뉴 건너뛰기




Volumn 111, Issue 13, 1998, Pages 1813-1821

The single CH domain of calponin is neither sufficient nor necessary for F-actin binding

Author keywords

Basic calponin isoform (h1); Calponin; CH domain; Localisation; Neutral calponin isoform (h2); Transfection

Indexed keywords

ACTIN BINDING PROTEIN; CALPONIN; F ACTIN;

EID: 0031822886     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (139)

References (51)
  • 1
    • 0028365640 scopus 로고
    • Cloning and expression of a novel acidic calponin isoform from aortic vascuar smooth muscle
    • Applegate, D., Feng, W., Green, R. S., and Taubman, M. B. (1994). Cloning and expression of a novel acidic calponin isoform from aortic vascuar smooth muscle. J. Biol. Chem. 269, 10683-10690.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10683-10690
    • Applegate, D.1    Feng, W.2    Green, R.S.3    Taubman, M.B.4
  • 2
    • 0030929148 scopus 로고    scopus 로고
    • IQGAP, a Rac- And Cdc 42-binding protein directly binds and cross-links microfilaments
    • Bashour, A.-M., Fullerton, A. T., Hart, M. J. and Bloom, G. S. (1997). IQGAP, a Rac- and Cdc 42-binding protein directly binds and cross-links microfilaments. J. Cell Biol. 137, 1555-1566.
    • (1997) J. Cell Biol. , vol.137 , pp. 1555-1566
    • Bashour, A.-M.1    Fullerton, A.T.2    Hart, M.J.3    Bloom, G.S.4
  • 3
    • 0029080918 scopus 로고
    • Interaction of smooth muscle calponin with phospholipids
    • Bogatcheva, N. V. and Gusev, N. B. (1995). Interaction of smooth muscle calponin with phospholipids. FEBS Lett. 371, 123-126.
    • (1995) FEBS Lett. , vol.371 , pp. 123-126
    • Bogatcheva, N.V.1    Gusev, N.B.2
  • 4
    • 0029784514 scopus 로고    scopus 로고
    • The RasGTPase-activating-protein-related human protein IQGAP 2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases
    • Brill, S., Li, S., Lyman, C. W., Church, D. M., Wasmuth, J. J., Weissbach, L., Bernards, A. and Snijders, A. J. (1996). The RasGTPase-activating-protein-related human protein IQGAP 2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol. Cell Biol. 16, 4869-4878.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4869-4878
    • Brill, S.1    Li, S.2    Lyman, C.W.3    Church, D.M.4    Wasmuth, J.J.5    Weissbach, L.6    Bernards, A.7    Snijders, A.J.8
  • 5
    • 0031040068 scopus 로고    scopus 로고
    • Crystal structure of a calponin homology domain
    • Carugo, K. D., Bañuelos, S. and Saraste, M. (1997). Crystal structure of a calponin homology domain. Nat. Struct. Biol. 4, 175-179.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 175-179
    • Carugo, K.D.1    Bañuelos, S.2    Saraste, M.3
  • 6
    • 0028785252 scopus 로고
    • Does vav bind to F-actin through a CH-domain?
    • Castresana, J. and Saraste, M. (1995). Does vav bind to F-actin through a CH-domain? FEBS Lett. 374, 149-151.
    • (1995) FEBS Lett. , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 7
    • 0029903722 scopus 로고    scopus 로고
    • The effect of smooth muscle calponin on the strong and weak binding sites of F-actin
    • EL-Mezgueldi, M. and Marston, S. B. (1996). The effect of smooth muscle calponin on the strong and weak binding sites of F-actin. J. Biol. Chem. 271, 28161-28167.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28161-28167
    • El-Mezgueldi, M.1    Marston, S.B.2
  • 8
    • 0029878648 scopus 로고    scopus 로고
    • Expressing functional domains of mouse calponin: Involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin
    • EL-Mezgueldi, M., Strasser, P., Fattoum, A. and Gimona, M. (1996). Expressing functional domains of mouse calponin: involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin. Biochemistry 35, 3654-3661.
    • (1996) Biochemistry , vol.35 , pp. 3654-3661
    • El-Mezgueldi, M.1    Strasser, P.2    Fattoum, A.3    Gimona, M.4
  • 9
  • 11
    • 0030765098 scopus 로고    scopus 로고
    • Interaction of chicken gizzard smooth muscle calponin with brain microtubules
    • Fujii, T., Hiromori, T., Hamamoto, M. and Suzuki, T. (1997). Interaction of chicken gizzard smooth muscle calponin with brain microtubules. J. Biochem. (Tokyo) 122, 344-351.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 344-351
    • Fujii, T.1    Hiromori, T.2    Hamamoto, M.3    Suzuki, T.4
  • 15
  • 16
    • 0028822231 scopus 로고
    • Specificity of dimer formation in tropomyosins: Influence of alternatively spliced exons on homodimer and heterodimer assembly
    • Gimona, M., Watakabe, A. and Helfman, D. M. (1995). Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Natl. Acad. Sci. USA 92, 9776-9780.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9776-9780
    • Gimona, M.1    Watakabe, A.2    Helfman, D.M.3
  • 18
    • 0027968795 scopus 로고
    • The Caenorhabdites elegans UNC-87 protein is essential for maintenance, but not assembly, of body wall muscle
    • Goetinck, S. and Waterston, R. H. (1994a). The Caenorhabdites elegans UNC-87 protein is essential for maintenance, but not assembly, of body wall muscle. J. Cell Biol. 127, 71-78.
    • (1994) J. Cell Biol. , vol.127 , pp. 71-78
    • Goetinck, S.1    Waterston, R.H.2
  • 19
    • 0027982276 scopus 로고
    • The Caenorhabdites elegans muscle affecting gene unc-87 encodes a novel thin filament-associated protein
    • Goetinck, S. and Waterston, R. H. (1994b). The Caenorhabdites elegans muscle affecting gene unc-87 encodes a novel thin filament-associated protein. J. Cell Biol. 127, 79-93.
    • (1994) J. Cell Biol. , vol.127 , pp. 79-93
    • Goetinck, S.1    Waterston, R.H.2
  • 21
    • 0027382212 scopus 로고
    • Characterization of wild-type and mutant chicken gizzard α-calponin expressed in E. coli
    • Gong, B. J., Mabuchi, K., Takahashi, K., Nadal-Ginard, B. and Tao, T. (1993). Characterization of wild-type and mutant chicken gizzard α-calponin expressed in E. coli. J. Biochem (Tokyo) 114, 453-456.
    • (1993) J. Biochem (Tokyo) , vol.114 , pp. 453-456
    • Gong, B.J.1    Mabuchi, K.2    Takahashi, K.3    Nadal-Ginard, B.4    Tao, T.5
  • 22
    • 0029806812 scopus 로고    scopus 로고
    • Strong interaction between caldesmon and calponin
    • Graceffa, P., Adam, L. P. and Morgan, K. G. (1996). Strong interaction between caldesmon and calponin. J. Biol. Chem. 271, 30336-30339.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30336-30339
    • Graceffa, P.1    Adam, L.P.2    Morgan, K.G.3
  • 23
    • 0030727339 scopus 로고    scopus 로고
    • Evidence for a conformational change in actin induced by fimbrin (N375) binding
    • Hanein, D., Matsudaira, P. and DeRosier, D. J. (1997). Evidence for a conformational change in actin induced by fimbrin (N375) binding. J. Cell Biol. 139, 387-396.
    • (1997) J. Cell Biol. , vol.139 , pp. 387-396
    • Hanein, D.1    Matsudaira, P.2    Derosier, D.J.3
  • 24
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP 1. a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs
    • Hart, M. J., Callow, M. G., Souza, B. and Polakis, P. (1996). IQGAP 1. a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs. EMBO J. 15, 2997-3005.
    • (1996) EMBO J. , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 25
    • 0031576324 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments containing calponin: Visualization of interactions between F-actin and calponin
    • Hodgkinson, J. L., EL-Mezgueldi, M., Craig, R., Vibert, P., Marston, S. B. and Lehman, W. (1997). Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments containing calponin: visualization of interactions between F-actin and calponin. J. Mol. Biol. 273, 150-159.
    • (1997) J. Mol. Biol. , vol.273 , pp. 150-159
    • Hodgkinson, J.L.1    El-Mezgueldi, M.2    Craig, R.3    Vibert, P.4    Marston, S.B.5    Lehman, W.6
  • 26
    • 0026031054 scopus 로고
    • Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential
    • Katzav, S., Cleveland, J. L., Heslop, H. E. and Pulido, D. (1991). Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential. Mol. Cell Biol. 11, 1912-1920.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 1912-1920
    • Katzav, S.1    Cleveland, J.L.2    Heslop, H.E.3    Pulido, D.4
  • 27
    • 0023644595 scopus 로고
    • Isolation and characterization of an abundant and novel 22-kDa protein (SM 22) from chicken gizzard smooth muscle
    • Lees-Miller, J. P., Heeley, D. H., Smillie, L. B. and Kay, C. M. (1987). Isolation and characterization of an abundant and novel 22-kDa protein (SM 22) from chicken gizzard smooth muscle. J. Biol. Chem. 262, 2988-2993.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2988-2993
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3    Kay, C.M.4
  • 28
    • 0030923431 scopus 로고    scopus 로고
    • Association of calponin with desmin intermediate filaments
    • Mabuchi, K., Li, B., Ip, W. and Tao, T. (1997). Association of calponin with desmin intermediate filaments. J. Biol. Chem. 272, 22662-22666.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22662-22666
    • Mabuchi, K.1    Li, B.2    Ip, W.3    Tao, T.4
  • 30
    • 0026034515 scopus 로고
    • Molecular organization of actin crosslinking proteins
    • Matsudaira, P. (1991). Molecular organization of actin crosslinking proteins. Trends Biochem. Sci. 16, 87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 31
    • 0028176006 scopus 로고
    • Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough, A., Way, M. and DeRosiers, D. (1994). Determination of the α-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126, 433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    Derosiers, D.3
  • 32
    • 0026780387 scopus 로고
    • Mapping of the functional domains in the amino-terminal region of calponin
    • Mezgueldi, M., Fattoum, A., Derancourt, J. and Kassab, R. (1992). Mapping of the functional domains in the amino-terminal region of calponin. J. Biol. Chem. 267, 15943-15951.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15943-15951
    • Mezgueldi, M.1    Fattoum, A.2    Derancourt, J.3    Kassab, R.4
  • 33
    • 0028933882 scopus 로고
    • Characterization of the regulatory domain of gizzard calponin
    • Mezgueldi, M., Mendre, C., Calas, B., Kassab, R. and Fattoum, A. (1995). Characterization of the regulatory domain of gizzard calponin. J. Biol. Chem. 270, 8867-8876
    • (1995) J. Biol. Chem. , vol.270 , pp. 8867-8876
    • Mezgueldi, M.1    Mendre, C.2    Calas, B.3    Kassab, R.4    Fattoum, A.5
  • 34
    • 0032518319 scopus 로고    scopus 로고
    • Two distinct actin-binding sites of smooth muscle calponin
    • Minto, T., Yiasa, U., Nakamura, F., Naka, M. and Tanaka, T. (1998). Two distinct actin-binding sites of smooth muscle calponin. Eur. J. Biochem. 251, 262-268.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 262-268
    • Minto, T.1    Yiasa, U.2    Nakamura, F.3    Naka, M.4    Tanaka, T.5
  • 35
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signalling proteins
    • Musacchio, A., Gibson, T., Rice, P., Thompson, J. and Saraste, M. (1993). The PH domain: a common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci. 18, 343-348.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Saraste, M.5
  • 36
    • 0028265170 scopus 로고
    • Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells
    • North, A., Gimona, M., Cross, R. A. and Small, J. V. (1994). Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells. J. Cell Sci. 107, 437-444.
    • (1994) J. Cell Sci. , vol.107 , pp. 437-444
    • North, A.1    Gimona, M.2    Cross, R.A.3    Small, J.V.4
  • 38
    • 0028170812 scopus 로고
    • Structure of actin binding proteins: Insights about function at atomic resolution
    • Pollard, T. D., Almo, S., Quirk, S., Vinson, V. and Lattman, E. E. (1994). Structure of actin binding proteins: insights about function at atomic resolution. Annu. Rev. Cell Biol. 10, 207-249.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 207-249
    • Pollard, T.D.1    Almo, S.2    Quirk, S.3    Vinson, V.4    Lattman, E.E.5
  • 39
    • 0030446675 scopus 로고    scopus 로고
    • Structure and function of Vav
    • Romero, F. and Fischer, S. (1996). Structure and function of Vav. Cell. Signal. 8, 545-553.
    • (1996) Cell. Signal. , vol.8 , pp. 545-553
    • Romero, F.1    Fischer, S.2
  • 42
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction
    • Spudich, J. A. and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 44
    • 0016795559 scopus 로고
    • Changes in the state of actin during superprecipitation of actomyosin
    • Strzelecka-Golaszewska, H., Kakubiak, M. and Drabikowski, W. (1975). Changes in the state of actin during superprecipitation of actomyosin. Eur. J. Biochem. 55, 221-230.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 221-230
    • Strzelecka-Golaszewska, H.1    Kakubiak, M.2    Drabikowski, W.3
  • 45
    • 0027146195 scopus 로고
    • Interaction between calponin and smooth muscle myosin
    • Szymanski, P. and Tao, T. (1993). Interaction between calponin and smooth muscle myosin. FEBS Lett. 331, 256-259.
    • (1993) FEBS Lett. , vol.331 , pp. 256-259
    • Szymanski, P.1    Tao, T.2
  • 46
    • 0030936114 scopus 로고    scopus 로고
    • Localization of protein regions involved in the interaction between calponin and myosin
    • Szymanski, P. T. and Tao, T. (1997). Localization of protein regions involved in the interaction between calponin and myosin. J. Biol. Chem. 272, 11142-11146.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11142-11146
    • Szymanski, P.T.1    Tao, T.2
  • 47
  • 48
    • 0025879757 scopus 로고
    • Molecular cloning and sequence analysis of smooth muscle calponin
    • Takahashi, K. and Nadal-Ginard (1991). Molecular cloning and sequence analysis of smooth muscle calponin. J. Biol Chem. 266, 13284-13288.
    • (1991) J. Biol Chem. , vol.266 , pp. 13284-13288
    • Takahashi, K.1    Nadal-Ginard2
  • 49
    • 0028821463 scopus 로고
    • Expression of an acidic isoform of calponin in rat brain: Western blots on one- Or two-dimensional gels and immunolocalization in cultured cells
    • Trabelsi-Terzidis, H., Fattoum, A., Represa, A., Dessi, F., Ben-Ari, Y. and der Terossian, E. (1995). Expression of an acidic isoform of calponin in rat brain: Western blots on one- or two-dimensional gels and immunolocalization in cultured cells. Biochem. J. 306, 211-215.
    • (1995) Biochem. J. , vol.306 , pp. 211-215
    • Trabelsi-Terzidis, H.1    Fattoum, A.2    Represa, A.3    Dessi, F.4    Ben-Ari, Y.5    Der Terossian, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.